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Open data
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Basic information
| Entry | Database: PDB / ID: 4ybq | ||||||
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| Title | Rat GLUT5 with Fv in the outward-open form | ||||||
Components |
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Keywords | TRANSPORT PROTEIN/IMMUNE SYSTEM / SUGAR TRANSPORTER / MAJOR FACILITATOR SUPERFAMILY / TRANSPORT PROTEIN-IMMUNE SYSTEM complex | ||||||
| Function / homology | Function and homology informationIntestinal hexose absorption / regulation of systemic arterial blood pressure mediated by a chemical signal / fructose transmembrane transporter activity / fructose import across plasma membrane / fructose transmembrane transport / fructose binding / D-glucose transmembrane transporter activity / metanephric proximal tubule development / D-glucose transmembrane transport / cellular response to fructose stimulus ...Intestinal hexose absorption / regulation of systemic arterial blood pressure mediated by a chemical signal / fructose transmembrane transporter activity / fructose import across plasma membrane / fructose transmembrane transport / fructose binding / D-glucose transmembrane transporter activity / metanephric proximal tubule development / D-glucose transmembrane transport / cellular response to fructose stimulus / response to fructose / Neutrophil degranulation / sarcolemma / apical plasma membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | ![]() ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.27 Å | ||||||
Authors | Nomura, N. / Shimamura, T. / Iwata, S. | ||||||
| Funding support | Japan, 1items
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Citation | Journal: Nature / Year: 2015Title: Structure and mechanism of the mammalian fructose transporter GLUT5 Authors: Nomura, N. / Verdon, G. / Kang, H.J. / Shimamura, T. / Nomura, Y. / Sonoda, Y. / Hussien, S.A. / Qureshi, A.A. / Coincon, M. / Sato, Y. / Abe, H. / Nakada-Nakura, Y. / Hino, T. / Arakawa, T. ...Authors: Nomura, N. / Verdon, G. / Kang, H.J. / Shimamura, T. / Nomura, Y. / Sonoda, Y. / Hussien, S.A. / Qureshi, A.A. / Coincon, M. / Sato, Y. / Abe, H. / Nakada-Nakura, Y. / Hino, T. / Arakawa, T. / Kusano-Arai, O. / Iwanari, H. / Murata, T. / Kobayashi, T. / Hamakubo, T. / Kasahara, M. / Iwata, S. / Drew, D. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 4ybq.cif.gz | 557.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4ybq.ent.gz | 467.2 KB | Display | PDB format |
| PDBx/mmJSON format | 4ybq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4ybq_validation.pdf.gz | 485 KB | Display | wwPDB validaton report |
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| Full document | 4ybq_full_validation.pdf.gz | 513.8 KB | Display | |
| Data in XML | 4ybq_validation.xml.gz | 48.1 KB | Display | |
| Data in CIF | 4ybq_validation.cif.gz | 64.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yb/4ybq ftp://data.pdbj.org/pub/pdb/validation_reports/yb/4ybq | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4yb9C ![]() 3o7qS S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 56425.801 Da / Num. of mol.: 2 / Mutation: N50Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Antibody | Mass: 13446.994 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Brevibacillus choshinensis (bacteria)#3: Antibody | Mass: 14863.454 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Brevibacillus choshinensis (bacteria)Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.62 Å3/Da / Density % sol: 66.07 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 33-35% PEG400, 0.12 M CaCl2, 0.1 M Tris-HCl pH8.0 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å |
| Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Nov 22, 2010 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 3.27→50 Å / Num. obs: 38017 / % possible obs: 99.9 % / Redundancy: 13 % / Net I/σ(I): 1.22 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 3O7Q Resolution: 3.27→36.491 Å / SU ML: 0.46 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 33.44 / Stereochemistry target values: ML
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.27→36.491 Å
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| Refine LS restraints |
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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X-RAY DIFFRACTION
Japan, 1items
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Brevibacillus choshinensis (bacteria)